Recombinant Rabbit Sarcoplasmic/endoplasmic reticulum calcium ATPase 1 (ATP2A1), partial

Code CSB-YP002332RB
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Source Yeast
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Code CSB-EP002332RB
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Source E.coli
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Code CSB-EP002332RB-B
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Source E.coli
Conjugate Avi-tag Biotinylated
E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code CSB-BP002332RB
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Source Baculovirus
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Code CSB-MP002332RB
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Source Mammalian cell
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Product Details

Purity
>85% (SDS-PAGE)
Target Names
ATP2A1
Uniprot No.
Alternative Names
ATP2A1Sarcoplasmic/endoplasmic reticulum calcium ATPase 1; SERCA1; SR Ca(2+)-ATPase 1; EC 7.2.2.10; Calcium pump 1; Calcium-transporting ATPase sarcoplasmic reticulum type; fast twitch skeletal muscle isoform; Endoplasmic reticulum class 1/2 Ca(2+) ATPase
Species
Oryctolagus cuniculus (Rabbit)
Protein Length
Partial
Tag Info
Tag type will be determined during the manufacturing process.
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Form
Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
Buffer before Lyophilization
Tris/PBS-based buffer, 6% Trehalose, pH 8.0
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet
Please contact us to get it.

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Target Background

Function
Key regulator of striated muscle performance by acting as the major Ca(2+) ATPase responsible for the reuptake of cytosolic Ca(2+) into the sarcoplasmic reticulum. Catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction.
Gene References into Functions
  1. the major SR membrane lipid PC is optimal for all steps and, unlike the other headgroups, contributes favorable electrostatics and non-electrostatic elements during the Ca-ATPase transition PMID: 29032359
  2. ATP-dependent Ca(2+) transport by SERCA in single giant unilamellar vesicles was detected directly using confocal fluorescence microscopy. PMID: 27815070
  3. Glycine 105 as Pivot for a Critical Knee-like Joint between Cytoplasmic and Transmembrane Segments of the Second Transmembrane Helix in Ca2+-ATPase.( PMID: 27733680
  4. Here we describe the methods to analyze these processes in the transport cycle with a representative member of P-type ATPase family, SERCA1a, sarco(endo)plasmic reticulum Ca(2+)-ATPase PMID: 26695035
  5. oligonucleotide-based drugs could be used to fine-tune SERCA function to counterbalance the extent of the pathological insults. PMID: 26292938
  6. Inhibition of the sarco/endoplasmic reticulum Ca2+-ATPase (SERCA1) by rutin derivatives. PMID: 25467059
  7. Infrared spectroscopy was used to characterise recombinant sarcoplasmic reticulum Ca2+-ATPase (SERCA1a). PMID: 24965041
  8. Data show that biselyngbyasides (BLSs) bind to the pump SERCA1a calcium ATPase near the cytoplasmic surface of the transmembrane region. PMID: 25957767
  9. Cell functions regulated by protein-protein interactions of the SERCA1a-sarcolipin complex is accomplished via s-palmitoylation and s-oleoylation of sarcolipin. PMID: 25301946
  10. Rescue of mutated SERCA1 to sarcoplasmic reticulum membrane can re-establish resting cytosolic Ca(2+) concentration and prevent the appearance of pathological signs of cattle pseudomyotonia PMID: 25288803
  11. Conformation of the SERCA1A calcium ATPase in the presence of different lipids. PMID: 25103814
  12. Ca(2+) and PLB phosphorylation relieve SERCA-PLB inhibition by distinct mechanisms, but both are achieved primarily by structural changes within the SERCA-PLB complex, not by dissociation of that complex. PMID: 24813991
  13. Phosphorylated phospholamban stabilizes a unique conformation of SERCA that is characterized by a compact architecture. PMID: 24138857
  14. Data suggest some phytoestrogenic flavonoids cooperate to inhibit SERCA, alter ATP binding properties of SERCA, and alter phosphorylation/dephosphorylation of SERCA by binding to several sites that are close to ATP binding site. PMID: 24238016
  15. Data suggest that phospholamban PLN's conformational equilibrium is central to maintain sarcoplasmic reticulum Ca(2+)-ATPase SERCA's apparent Ca(2+) affinity within a physiological window. PMID: 24101520
  16. Data suggest that the long-range electrostatics likely guide N and P domain motions in SERCA1a calcium ATPase. PMID: 23737524
  17. Sarcoplasmic reticulum Ca(2+) uptake by SERCA is an integral part of the mechanism by which spontaneous Ca(2+) waves propagate through cardiac myocytes. PMID: 22988145
  18. crystal structure of native SERCA1a (from rabbit) in this E1.Mg(2+) state at 3.0 A resolution in addition to crystal structures of SERCA1a in E2 free from exogenous inhibitors PMID: 23455422
  19. crystal structure of rabbit SERCA1a (also known as ATP2A1) in complex with sarcolipin at 3.1 A resolution PMID: 23455424
  20. CS and SERCA activities were significantly higher in the pubococcygeus (Pc) compared with the ischiocavernosus/bulbospongiosus (Ic/Bs) pelvic floor muscles, whereas the ChAT activity of the Ic/Bs was higher than that of the Pc muscle. PMID: 22911511
  21. On the basis of extended MD simulations with 8 combinations of protonation states of 4 acidic residues in the Ca2+ ion binding sites, data indicate 3 bound protons are sufficient to ensure a stable binding pocket in SERCA. PMID: 22082179
  22. The lipid bilayer composition influences the regulation of SERCA by PLN. PMID: 21992175
  23. Investigations visualize conformational changes in SERCA (in sarcoplasmic reticulum) in real time at single-molecule level. Data suggest catalytic pathway of SERCA is different from the ordinary Albers-Post scheme under physiological conditions. PMID: 21707923
  24. Curcumin could improve cardiac function via upregulating the expression of sarcoplasmic reticulum Ca2+-ATPase. PMID: 20654087
  25. the effects of substitution mutations on the isolated SERCA1a-nucleotide binding domain (SERCA-N) were studied using NMR. PMID: 21187073
  26. Phosphorylation of PLB induces spatial rearrangements between the N- and P-domain elements of proximal Ca-ATPase. PMID: 19191503
  27. Digestion with proteinase K or trypsin yields complementary information on conformational transitions of the Ca(2+)-ATPase (SERCA) in the native membrane environment PMID: 17993458

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Subcellular Location
Endoplasmic reticulum membrane; Multi-pass membrane protein. Sarcoplasmic reticulum membrane; Multi-pass membrane protein.
Protein Families
Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIA subfamily
Tissue Specificity
Skeletal muscle (at protein level). Skeletal muscle, fast twitch muscle (type II) fibers.
Database Links
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